| Tag | Content |
|---|
| CPLM ID | CPLM-023171 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Zinc finger and BTB domain-containing protein 21 |
Protein Synonyms/Alias | Zinc finger protein 295 |
Gene Name | ZBTB21 |
Gene Synonyms/Alias | KIAA1227; ZNF295 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 40 | LLIVGDQKFRAHKNV | sumoylation | [1] |
|
Reference | [1] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC. Mol Cell. 2010 Aug 27;39(4):641-52. [ PMID: 20797634] |
Functional Description | Acts as a transcription repressor. |
Sequence Annotation | DOMAIN 30 96 BTB.
ZN_FING 546 569 C2H2-type 1.
ZN_FING 575 598 C2H2-type 2.
ZN_FING 670 692 C2H2-type 3.
ZN_FING 748 770 C2H2-type 4; atypical.
ZN_FING 775 798 C2H2-type 5.
ZN_FING 909 932 C2H2-type 6; atypical.
ZN_FING 937 959 C2H2-type 7.
ZN_FING 1043 1065 C2H2-type 8.
REGION 30 96 Mediates homodimerization.
MOD_RES 381 381 Phosphoserine.
MOD_RES 411 411 Phosphoserine.
MOD_RES 422 422 Phosphoserine.
MOD_RES 431 431 Phosphothreonine.
MOD_RES 434 434 Phosphoserine.
MOD_RES 435 435 Phosphoserine.
MOD_RES 438 438 Phosphoserine.
MOD_RES 605 605 Phosphoserine.
MOD_RES 714 714 Phosphoserine.
MOD_RES 1003 1003 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1066 AA |
Protein Sequence | MEGLLHYINP AHAISLLSAL NEERLKGQLC DVLLIVGDQK FRAHKNVLAA SSEYFQSLFT 60
NKENESQTVF QLDFCEPDAF DNVLNYIYSS SLFVEKSSLA AVQELGYSLG ISFLTNIVSK 120
TPQAPFPTCP NRKKVFVEDD ENSSQKRSVI VCQSRNEAQG KTVSQNQPDV SHTSRPSPSI 180
AVKANTNKPH VPKPIEPLHN LSLTEKSWPK DSSVVYAKSL EHSGSLDDPN RISLVKRNAV 240
LPSKPLQDRE AMDDKPGVSG QLPKGKALEL ALKRPRPPVL SVCSSSETPY LLKETNKGNG 300
QGEDRNLLYY SKLGLVIPSS GSGSGNQSID RSGPLVKSLL RRSLSMDSQV PVYSPSIDLK 360
SSQGSSSVSS DAPGNVLCAL SQKSSLKDCS EKTALDDRPQ VLQPHRLRSF SASQSTDREG 420
ASPVTEVRIK TEPSSPLSDP SDIIRVTVGD AATTAAASSS SVTRDLSLKT EDDQKDMSRL 480
PAKRRFQADR RLPFKKLKVN EHGSPVSEDN FEEGSSPTLL DADFPDSDLN KDEFGELEGT 540
RPNKKFKCKH CLKIFRSTAG LHRHVNMYHN PEKPYACDIC HKRFHTNFKV WTHCQTQHGI 600
VKNPSPASSS HAVLDEKFQR KLIDIVRERE IKKALIIKLR RGKPGFQGQS SSQAQQVIKR 660
NLRSRAKGAY ICTYCGKAYR FLSQFKQHIK MHPGEKPLGV NKVAKPKEHA PLASPVENKE 720
VYQCRLCNAK LSSLLEQGSH ERLCRNAAVC PYCSLRFFSP ELKQEHESKC EYKKLTCLEC 780
MRTFKSSFSI WRHQVEVHNQ NNMAPTENFS LPVLDHNGDV TGSSRPQSQP EPNKVNHIVT 840
TKDDNVFSDS SEQVNFDSED SSCLPEDLSL SKQLKIQVKE EPVEEAEEEA PEASTAPKEA 900
GPSKEASLWP CEKCGKMFTV HKQLERHQEL LCSVKPFICH VCNKAFRTNF RLWSHFQSHM 960
SQASEESAHK ESEVCPVPTN SPSPPPLPPP PPLPKIQPLE PDSPTGLSEN PTPATEKLFV 1020
PQESDTLFYH APPLSAITFK RQFMCKLCHR TFKTAFSLWS HEQTHN 1066 |
Gene Ontology | GO:0005634; C:nucleus; IDA:UniProtKB. GO:0008327; F:methyl-CpG binding; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |